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<entry dataset="Swiss-Prot" created="2008-02-05" modified="2026-11-04" version="104" xmlns="http://uniprot.org/uniprot">
  <accession>Q0T9J7</accession>
  <name>ULAD_ECOL5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-keto-L-gulonate-6-phosphate decarboxylase UlaD</fullName>
      <ecNumber evidence="1">4.1.1.85</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">3-dehydro-L-gulonate-6-phosphate decarboxylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">KGPDC</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">L-ascorbate utilization protein D</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ulaD</name>
    <name type="ordered locus">ECP_4441</name>
  </gene>
  <organism>
    <name type="scientific">Escherichia coli O6:K15:H31 (strain 536 / UPEC)</name>
    <dbReference type="NCBI Taxonomy" id="362663"/>
    <lineage>
      <taxon>Bacteria</taxon>
      <taxon>Pseudomonadati</taxon>
      <taxon>Pseudomonadota</taxon>
      <taxon>Gammaproteobacteria</taxon>
      <taxon>Enterobacterales</taxon>
      <taxon>Enterobacteriaceae</taxon>
      <taxon>Escherichia</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="Mol. Microbiol." volume="61" first="584" last="595">
      <title>Role of pathogenicity island-associated integrases in the genome plasticity of uropathogenic Escherichia coli strain 536.</title>
      <authorList>
        <person name="Hochhut B."/>
        <person name="Wilde C."/>
        <person name="Balling G."/>
        <person name="Middendorf B."/>
        <person name="Dobrindt U."/>
        <person name="Brzuszkiewicz E."/>
        <person name="Gottschalk G."/>
        <person name="Carniel E."/>
        <person name="Hacker J."/>
      </authorList>
      <dbReference type="PubMed" id="16879640"/>
      <dbReference type="DOI" id="10.1111/j.1365-2958.2006.05255.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>536 / UPEC</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the decarboxylation of 3-keto-L-gulonate-6-P into L-xylulose-5-P. Is involved in the anaerobic L-ascorbate utilization.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-dehydro-L-gulonate 6-phosphate + H(+) = L-xylulose 5-phosphate + CO2</text>
      <dbReference type="Rhea" id="RHEA:14353"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:57829"/>
      <dbReference type="ChEBI" id="CHEBI:58774"/>
      <dbReference type="EC" id="4.1.1.85"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds 1 Mg(2+) ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor degradation; L-ascorbate degradation; D-xylulose 5-phosphate from L-ascorbate: step 2/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="induction">
    <text evidence="1">Induced by L-ascorbate. Repressed by UlaR.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the HPS/KGPDC family. KGPDC subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.85" evidence="1"/>
  <dbReference type="EMBL" id="CP000247">
    <property type="protein sequence ID" value="ABG72382.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_000056749.1">
    <property type="nucleotide sequence ID" value="NC_008253.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q0T9J7"/>
  <dbReference type="SMR" id="Q0T9J7"/>
  <dbReference type="KEGG" id="ecp:ECP_4441"/>
  <dbReference type="HOGENOM" id="CLU_081825_0_0_6"/>
  <dbReference type="OMA" id="AARDFKN"/>
  <dbReference type="UniPathway" id="UPA00263">
    <property type="reaction ID" value="UER00378"/>
  </dbReference>
  <dbReference type="GO" id="GO:0033982">
    <property type="term" value="F:3-dehydro-L-gulonate-6-phosphate decarboxylase activity"/>
    <property type="evidence" value="ECO:0000501"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0000501"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004590">
    <property type="term" value="F:orotidine-5'-phosphate decarboxylase activity"/>
    <property type="evidence" value="ECO:0000501"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006207">
    <property type="term" value="P:'de novo' pyrimidine nucleobase biosynthetic process"/>
    <property type="evidence" value="ECO:0000501"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019854">
    <property type="term" value="P:L-ascorbic acid catabolic process"/>
    <property type="evidence" value="ECO:0000501"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd04726">
    <property type="entry name" value="KGPDC_HPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="FunFam" id="3.20.20.70:FF:000022">
    <property type="entry name" value="3-keto-L-gulonate-6-phosphate decarboxylase UlaD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="entry name" value="Aldolase class I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01267">
    <property type="entry name" value="UlaD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023942">
    <property type="entry name" value="3-keto-L-gulonate6Pdecase_UlaD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041710">
    <property type="entry name" value="HPS/KGPDC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001754">
    <property type="entry name" value="OMPdeCOase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011060">
    <property type="entry name" value="RibuloseP-bd_barrel"/>
  </dbReference>
  <dbReference type="NCBIfam" id="NF009832">
    <property type="entry name" value="PRK13306.1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35039">
    <property type="entry name" value="3-KETO-L-GULONATE-6-PHOSPHATE DECARBOXYLASE SGBH-RELATED"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35039:SF3">
    <property type="entry name" value="3-KETO-L-GULONATE-6-PHOSPHATE DECARBOXYLASE SGBH-RELATED"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00215">
    <property type="entry name" value="OMPdecase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00934">
    <property type="entry name" value="OMPdecase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51366">
    <property type="entry name" value="Ribulose-phoshate binding barrel"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0119">Carbohydrate metabolism</keyword>
  <keyword id="KW-0210">Decarboxylase</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <feature type="chain" id="PRO_1000067320" description="3-keto-L-gulonate-6-phosphate decarboxylase UlaD">
    <location>
      <begin position="1"/>
      <end position="216"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="11"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="33"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="62"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="192"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="64"/>
    </location>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="67"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01267"/>
    </source>
  </evidence>
  <sequence length="216" mass="23578" checksum="EC8490DA1D02D824" modified="2006-09-05" version="1">MSLPMLQVALDNQTMDSAYETTRLIAEEVDIIEVGTILCVGEGVRAVRDLKALYPHKIVLADAKIADAGKILSRMCFEANADWVTVICCADINTAKGALDVAKEFNGDVQIELTGYWTWEQAQQWRDAGIGQVVYHRSRDAQAAGVAWGEADITAIKRLSDMGFKVTVTGGLALEDLPLFKGIPIHVFIAGRSIRDAASPVEAARQFKRSIAELWG</sequence>
</entry>
<copyright>
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms Distributed under the Creative Commons Attribution (CC BY 4.0) License
</copyright>
</uniprot>